Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P09110

- THIK_HUMAN

UniProt

P09110 - THIK_HUMAN

Protein

3-ketoacyl-CoA thiolase, peroxisomal

Gene

ACAA1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 167 (01 Oct 2014)
      Sequence version 2 (01 Oct 1989)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Catalytic activityi

    Acyl-CoA + acetyl-CoA = CoA + 3-oxoacyl-CoA.

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei123 – 1231Acyl-thioester intermediateBy similarity
    Active sitei377 – 3771Proton acceptorPROSITE-ProRule annotation
    Active sitei408 – 4081Proton acceptorPROSITE-ProRule annotation

    GO - Molecular functioni

    1. acetyl-CoA C-acyltransferase activity Source: UniProtKB-EC
    2. palmitoyl-CoA oxidase activity Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. alpha-linolenic acid metabolic process Source: Reactome
    2. bile acid metabolic process Source: UniProtKB
    3. cellular lipid metabolic process Source: Reactome
    4. fatty acid beta-oxidation Source: UniProtKB
    5. fatty acid beta-oxidation using acyl-CoA oxidase Source: Reactome
    6. small molecule metabolic process Source: Reactome
    7. unsaturated fatty acid metabolic process Source: Reactome
    8. very long-chain fatty acid metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Acyltransferase, Transferase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:HS00752-MONOMER.
    ReactomeiREACT_121147. alpha-linolenic acid (ALA) metabolism.
    REACT_17062. Beta-oxidation of very long chain fatty acids.
    UniPathwayiUPA00199.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-ketoacyl-CoA thiolase, peroxisomal (EC:2.3.1.16)
    Alternative name(s):
    Acetyl-CoA acyltransferase
    Beta-ketothiolase
    Peroxisomal 3-oxoacyl-CoA thiolase
    Gene namesi
    Name:ACAA1
    Synonyms:ACAA, PTHIO
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:82. ACAA1.

    Subcellular locationi

    GO - Cellular componenti

    1. intracellular membrane-bounded organelle Source: HPA
    2. membrane Source: UniProtKB
    3. peroxisomal matrix Source: Reactome
    4. peroxisome Source: UniProtKB

    Keywords - Cellular componenti

    Peroxisome

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA24419.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2626PeroxisomeAdd
    BLAST
    Chaini27 – 4243983-ketoacyl-CoA thiolase, peroxisomalPRO_0000034067Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei59 – 591Phosphothreonine1 Publication
    Modified residuei60 – 601Phosphothreonine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiP09110.
    PaxDbiP09110.
    PeptideAtlasiP09110.
    PRIDEiP09110.

    2D gel databases

    REPRODUCTION-2DPAGEIPI00012828.
    UCD-2DPAGEP09110.

    PTM databases

    PhosphoSiteiP09110.

    Expressioni

    Inductioni

    Peroxisomal thiolase is markedly induced (at the level of transcription) by various hypolipidemic compounds in parallel with the other two enzymes of the peroxisomal beta-oxidation system.

    Gene expression databases

    ArrayExpressiP09110.
    BgeeiP09110.
    CleanExiHS_ACAA1.
    GenevestigatoriP09110.

    Organism-specific databases

    HPAiHPA006764.
    HPA007244.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi106548. 18 interactions.
    IntActiP09110. 1 interaction.
    MINTiMINT-3006670.
    STRINGi9606.ENSP00000333664.

    Structurei

    Secondary structure

    1
    424
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi38 – 458
    Turni51 – 533
    Turni55 – 584
    Helixi61 – 7616
    Helixi80 – 823
    Beta strandi86 – 894
    Beta strandi91 – 944
    Helixi95 – 973
    Helixi98 – 10710
    Beta strandi116 – 1205
    Helixi122 – 1243
    Helixi125 – 13814
    Beta strandi143 – 15210
    Turni153 – 1553
    Helixi168 – 1703
    Helixi172 – 1754
    Helixi176 – 1783
    Helixi181 – 19111
    Helixi196 – 21621
    Turni217 – 2226
    Beta strandi226 – 2316
    Beta strandi237 – 2426
    Helixi254 – 2596
    Beta strandi263 – 2653
    Beta strandi279 – 28911
    Helixi290 – 2967
    Beta strandi302 – 31110
    Helixi314 – 3196
    Helixi320 – 33213
    Helixi336 – 3383
    Beta strandi339 – 3446
    Helixi349 – 35911
    Helixi363 – 3653
    Helixi372 – 3754
    Turni379 – 3813
    Helixi382 – 39716
    Beta strandi401 – 4099
    Turni410 – 4123
    Beta strandi413 – 4219

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2IIKX-ray2.55A/B30-423[»]
    ProteinModelPortaliP09110.
    SMRiP09110. Positions 28-424.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09110.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the thiolase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0183.
    HOGENOMiHOG000012239.
    HOVERGENiHBG003112.
    InParanoidiP09110.
    KOiK07513.
    OMAiACTREWG.
    OrthoDBiEOG7K3TM6.
    PhylomeDBiP09110.
    TreeFamiTF332308.

    Family and domain databases

    Gene3Di3.40.47.10. 4 hits.
    InterProiIPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view]
    PfamiPF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view]
    PIRSFiPIRSF000429. Ac-CoA_Ac_transf. 1 hit.
    SUPFAMiSSF53901. SSF53901. 2 hits.
    TIGRFAMsiTIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEiPS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P09110-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MQRLQVVLGH LRGPADSGWM PQAAPCLSGA PQASAADVVV VHGRRTAICR    50
    AGRGGFKDTT PDELLSAVMT AVLKDVNLRP EQLGDICVGN VLQPGAGAIM 100
    ARIAQFLSDI PETVPLSTVN RQCSSGLQAV ASIAGGIRNG SYDIGMACGV 150
    ESMSLADRGN PGNITSRLME KEKARDCLIP MGITSENVAE RFGISREKQD 200
    TFALASQQKA ARAQSKGCFQ AEIVPVTTTV HDDKGTKRSI TVTQDEGIRP 250
    STTMEGLAKL KPAFKKDGST TAGNSSQVSD GAAAILLARR SKAEELGLPI 300
    LGVLRSYAVV GVPPDIMGIG PAYAIPVALQ KAGLTVSDVD IFEINEAFAS 350
    QAAYCVEKLR LPPEKVNPLG GAVALGHPLG CTGARQVITL LNELKRRGKR 400
    AYGVVSMCIG TGMGAAAVFE YPGN 424
    Length:424
    Mass (Da):44,292
    Last modified:October 1, 1989 - v2
    Checksum:i71B2BBAFA06AE412
    GO
    Isoform 2 (identifier: P09110-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         149-181: Missing.
         272-331: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:331
    Mass (Da):34,665
    Checksum:i8137A0AC448FBA24
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti172 – 1721E → D.
    Corresponds to variant rs156265 [ dbSNP | Ensembl ].
    VAR_011904
    Natural varianti387 – 3871V → A.1 Publication
    Corresponds to variant rs2229528 [ dbSNP | Ensembl ].
    VAR_069148

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei149 – 18133Missing in isoform 2. 1 PublicationVSP_046195Add
    BLAST
    Alternative sequencei272 – 33160Missing in isoform 2. 1 PublicationVSP_046196Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12966 mRNA. Translation: CAA31412.1.
    X14813 mRNA. Translation: CAA32918.1.
    X65140 Genomic DNA. Translation: CAA46270.1.
    X65148 Genomic DNA. Translation: CAA46271.1.
    AP006309 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64516.1.
    BC000635 mRNA. Translation: AAH00635.1.
    BC011977 mRNA. Translation: AAH11977.1.
    BC014474 mRNA. Translation: AAH14474.1.
    CCDSiCCDS2673.1. [P09110-1]
    CCDS46794.1. [P09110-2]
    PIRiS17515. XUHUAB.
    RefSeqiNP_001123882.1. NM_001130410.1. [P09110-2]
    NP_001598.1. NM_001607.3. [P09110-1]
    UniGeneiHs.643487.

    Genome annotation databases

    EnsembliENST00000301810; ENSP00000301810; ENSG00000060971. [P09110-2]
    ENST00000333167; ENSP00000333664; ENSG00000060971. [P09110-1]
    GeneIDi30.
    KEGGihsa:30.
    UCSCiuc003cht.3. human. [P09110-1]
    uc003chu.3. human.

    Polymorphism databases

    DMDMi135751.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X12966 mRNA. Translation: CAA31412.1 .
    X14813 mRNA. Translation: CAA32918.1 .
    X65140 Genomic DNA. Translation: CAA46270.1 .
    X65148 Genomic DNA. Translation: CAA46271.1 .
    AP006309 Genomic DNA. No translation available.
    CH471055 Genomic DNA. Translation: EAW64516.1 .
    BC000635 mRNA. Translation: AAH00635.1 .
    BC011977 mRNA. Translation: AAH11977.1 .
    BC014474 mRNA. Translation: AAH14474.1 .
    CCDSi CCDS2673.1. [P09110-1 ]
    CCDS46794.1. [P09110-2 ]
    PIRi S17515. XUHUAB.
    RefSeqi NP_001123882.1. NM_001130410.1. [P09110-2 ]
    NP_001598.1. NM_001607.3. [P09110-1 ]
    UniGenei Hs.643487.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2IIK X-ray 2.55 A/B 30-423 [» ]
    ProteinModelPortali P09110.
    SMRi P09110. Positions 28-424.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 106548. 18 interactions.
    IntActi P09110. 1 interaction.
    MINTi MINT-3006670.
    STRINGi 9606.ENSP00000333664.

    PTM databases

    PhosphoSitei P09110.

    Polymorphism databases

    DMDMi 135751.

    2D gel databases

    REPRODUCTION-2DPAGE IPI00012828.
    UCD-2DPAGE P09110.

    Proteomic databases

    MaxQBi P09110.
    PaxDbi P09110.
    PeptideAtlasi P09110.
    PRIDEi P09110.

    Protocols and materials databases

    DNASUi 30.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000301810 ; ENSP00000301810 ; ENSG00000060971 . [P09110-2 ]
    ENST00000333167 ; ENSP00000333664 ; ENSG00000060971 . [P09110-1 ]
    GeneIDi 30.
    KEGGi hsa:30.
    UCSCi uc003cht.3. human. [P09110-1 ]
    uc003chu.3. human.

    Organism-specific databases

    CTDi 30.
    GeneCardsi GC03M038164.
    HGNCi HGNC:82. ACAA1.
    HPAi HPA006764.
    HPA007244.
    MIMi 604054. gene.
    neXtProti NX_P09110.
    PharmGKBi PA24419.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0183.
    HOGENOMi HOG000012239.
    HOVERGENi HBG003112.
    InParanoidi P09110.
    KOi K07513.
    OMAi ACTREWG.
    OrthoDBi EOG7K3TM6.
    PhylomeDBi P09110.
    TreeFami TF332308.

    Enzyme and pathway databases

    UniPathwayi UPA00199 .
    BioCyci MetaCyc:HS00752-MONOMER.
    Reactomei REACT_121147. alpha-linolenic acid (ALA) metabolism.
    REACT_17062. Beta-oxidation of very long chain fatty acids.

    Miscellaneous databases

    ChiTaRSi ACAA1. human.
    EvolutionaryTracei P09110.
    GeneWikii ACAA1.
    GenomeRNAii 30.
    NextBioi 107.
    PROi P09110.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09110.
    Bgeei P09110.
    CleanExi HS_ACAA1.
    Genevestigatori P09110.

    Family and domain databases

    Gene3Di 3.40.47.10. 4 hits.
    InterProi IPR002155. Thiolase.
    IPR016039. Thiolase-like.
    IPR016038. Thiolase-like_subgr.
    IPR020615. Thiolase_acyl_enz_int_AS.
    IPR020610. Thiolase_AS.
    IPR020617. Thiolase_C.
    IPR020613. Thiolase_CS.
    IPR020616. Thiolase_N.
    [Graphical view ]
    Pfami PF02803. Thiolase_C. 1 hit.
    PF00108. Thiolase_N. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF000429. Ac-CoA_Ac_transf. 1 hit.
    SUPFAMi SSF53901. SSF53901. 2 hits.
    TIGRFAMsi TIGR01930. AcCoA-C-Actrans. 1 hit.
    PROSITEi PS00098. THIOLASE_1. 1 hit.
    PS00737. THIOLASE_2. 1 hit.
    PS00099. THIOLASE_3. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Nucleotide sequence of human peroxisomal 3-oxoacyl-CoA thiolase."
      Bout A., Teunissen Y., Hashimoto T., Benne R., Tager J.M.
      Nucleic Acids Res. 16:10369-10369(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    2. Bout A.
      Submitted (AUG-1989) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION TO 285-287.
    3. "Complete cDNA sequence of human foetal liver peroxisomal 3-oxoacyl-CoA thiolase."
      Fairbairn L.J., Tanner M.J.A.
      Nucleic Acids Res. 17:3588-3588(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
      Tissue: Liver.
    4. "Characterization of the gene encoding human peroxisomal 3-oxoacyl-CoA thiolase (ACAA). No large DNA rearrangement in a thiolase-deficient patient."
      Bout A., Franse M.M., Collins J., Blonden L., Tager J.M., Benne R.
      Biochim. Biophys. Acta 1090:43-51(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    5. "The DNA sequence, annotation and analysis of human chromosome 3."
      Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
      , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
      Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), VARIANT ALA-387.
      Tissue: Lymph, Ovary and Pancreas.
    8. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-59 AND THR-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    10. "Crystal structure of human peroxisomal acetyl-COA acyl transferase 1 (ACAA1)."
      Structural genomics consortium (SGC)
      Submitted (OCT-2006) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 28-424, SUBUNIT.

    Entry informationi

    Entry nameiTHIK_HUMAN
    AccessioniPrimary (citable) accession number: P09110
    Secondary accession number(s): G5E935, Q96CA6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: October 1, 1989
    Last modified: October 1, 2014
    This is version 167 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 3
      Human chromosome 3: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    6. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    7. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3